MULTISPECIES: formyltetrahydrofolate deformylase [Acinetobacter]
Protein Classification
formyltetrahydrofolate deformylase( domain architecture ID 11481955)
formyltetrahydrofolate deformylase catalyzes the hydrolysis of 10-formyltetrahydrofolate (formyl-FH4) to tetrahydrofolate (FH4) and formate
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| purU | PRK06027 | formyltetrahydrofolate deformylase; Reviewed |
3-287 | 2.90e-173 | |||||
formyltetrahydrofolate deformylase; Reviewed : Pssm-ID: 235676 [Multi-domain] Cd Length: 286 Bit Score: 479.99 E-value: 2.90e-173
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| Name | Accession | Description | Interval | E-value | |||||
| purU | PRK06027 | formyltetrahydrofolate deformylase; Reviewed |
3-287 | 2.90e-173 | |||||
formyltetrahydrofolate deformylase; Reviewed Pssm-ID: 235676 [Multi-domain] Cd Length: 286 Bit Score: 479.99 E-value: 2.90e-173
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| PurU | COG0788 | Formyltetrahydrofolate hydrolase [Nucleotide transport and metabolism]; Formyltetrahydrofolate ... |
7-287 | 8.43e-172 | |||||
Formyltetrahydrofolate hydrolase [Nucleotide transport and metabolism]; Formyltetrahydrofolate hydrolase is part of the Pathway/BioSystem: Purine biosynthesis Pssm-ID: 440551 [Multi-domain] Cd Length: 282 Bit Score: 476.08 E-value: 8.43e-172
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| PurU | TIGR00655 | formyltetrahydrofolate deformylase; This model describes formyltetrahydrofolate deformylases. ... |
9-287 | 2.15e-136 | |||||
formyltetrahydrofolate deformylase; This model describes formyltetrahydrofolate deformylases. The enzyme is a homohexamer. Sequences from a related enzyme formyl tetrahydrofolate-specific enzyme, phosphoribosylglycinamide formyltransferase, serve as an outgroup for phylogenetic analysis. Putative members of this family, scoring below the trusted cutoff, include a sequence from Rhodobacter capsulatus that lacks an otherwise conserved C-terminal region. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis] Pssm-ID: 273199 [Multi-domain] Cd Length: 280 Bit Score: 386.40 E-value: 2.15e-136
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| FMT_core_Formyl-FH4-Hydrolase_C | cd08648 | Formyltetrahydrofolate deformylase (Formyl-FH4 hydrolase), C-terminal hydrolase domain; ... |
94-287 | 4.01e-114 | |||||
Formyltetrahydrofolate deformylase (Formyl-FH4 hydrolase), C-terminal hydrolase domain; Formyl-FH4 Hydrolase catalyzes the hydrolysis of 10-formyltetrahydrofolate (formyl-FH4) to FH4 and formate. Formate is the substrate of phosphoribosylglycinamide transformylase for step three of de novo purine nucleotide synthesis. Formyl-FH4 hydrolase has been proposed to regulate the balance of FH4 and C1-FH4 in the cell. The enzyme uses methionine and glycine to sense the pools of C1-FH4 and FH4, respectively. This domain belongs to the formyltransferase (FMT) domain superfamily. Members of this family have an N-terminal ACT domain, which is commonly involved in specifically bind an amino acid or other small ligand leading to regulation of the enzyme. The N-terminal of this protein family may be responsible for the binding of the regulators methionine and glycine. Pssm-ID: 187717 [Multi-domain] Cd Length: 196 Bit Score: 326.83 E-value: 4.01e-114
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| Formyl_trans_N | pfam00551 | Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ... |
94-269 | 9.72e-41 | |||||
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide transformylase catalyzes the third step in de novo purine biosynthesis, the transfer of a formyl group to 5'-phosphoribosylglycinamide. Formyltetrahydrofolate deformylase produces formate from formyl- tetrahydrofolate. Methionyl-tRNA formyltransferase transfers a formyl group onto the amino terminus of the acyl moiety of the methionyl aminoacyl-tRNA. Inclusion of the following members is supported by PSI-blast. HOXX_BRAJA (P31907) contains a related domain of unknown function. PRTH_PORGI (P46071) contains a related domain of unknown function. Y09P_MYCTU (Q50721) contains a related domain of unknown function. Pssm-ID: 395436 [Multi-domain] Cd Length: 181 Bit Score: 139.35 E-value: 9.72e-41
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| Name | Accession | Description | Interval | E-value | |||||
| purU | PRK06027 | formyltetrahydrofolate deformylase; Reviewed |
3-287 | 2.90e-173 | |||||
formyltetrahydrofolate deformylase; Reviewed Pssm-ID: 235676 [Multi-domain] Cd Length: 286 Bit Score: 479.99 E-value: 2.90e-173
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| PurU | COG0788 | Formyltetrahydrofolate hydrolase [Nucleotide transport and metabolism]; Formyltetrahydrofolate ... |
7-287 | 8.43e-172 | |||||
Formyltetrahydrofolate hydrolase [Nucleotide transport and metabolism]; Formyltetrahydrofolate hydrolase is part of the Pathway/BioSystem: Purine biosynthesis Pssm-ID: 440551 [Multi-domain] Cd Length: 282 Bit Score: 476.08 E-value: 8.43e-172
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| PurU | TIGR00655 | formyltetrahydrofolate deformylase; This model describes formyltetrahydrofolate deformylases. ... |
9-287 | 2.15e-136 | |||||
formyltetrahydrofolate deformylase; This model describes formyltetrahydrofolate deformylases. The enzyme is a homohexamer. Sequences from a related enzyme formyl tetrahydrofolate-specific enzyme, phosphoribosylglycinamide formyltransferase, serve as an outgroup for phylogenetic analysis. Putative members of this family, scoring below the trusted cutoff, include a sequence from Rhodobacter capsulatus that lacks an otherwise conserved C-terminal region. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis] Pssm-ID: 273199 [Multi-domain] Cd Length: 280 Bit Score: 386.40 E-value: 2.15e-136
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| PRK13011 | PRK13011 | formyltetrahydrofolate deformylase; Reviewed |
11-288 | 3.22e-120 | |||||
formyltetrahydrofolate deformylase; Reviewed Pssm-ID: 237266 [Multi-domain] Cd Length: 286 Bit Score: 345.81 E-value: 3.22e-120
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| FMT_core_Formyl-FH4-Hydrolase_C | cd08648 | Formyltetrahydrofolate deformylase (Formyl-FH4 hydrolase), C-terminal hydrolase domain; ... |
94-287 | 4.01e-114 | |||||
Formyltetrahydrofolate deformylase (Formyl-FH4 hydrolase), C-terminal hydrolase domain; Formyl-FH4 Hydrolase catalyzes the hydrolysis of 10-formyltetrahydrofolate (formyl-FH4) to FH4 and formate. Formate is the substrate of phosphoribosylglycinamide transformylase for step three of de novo purine nucleotide synthesis. Formyl-FH4 hydrolase has been proposed to regulate the balance of FH4 and C1-FH4 in the cell. The enzyme uses methionine and glycine to sense the pools of C1-FH4 and FH4, respectively. This domain belongs to the formyltransferase (FMT) domain superfamily. Members of this family have an N-terminal ACT domain, which is commonly involved in specifically bind an amino acid or other small ligand leading to regulation of the enzyme. The N-terminal of this protein family may be responsible for the binding of the regulators methionine and glycine. Pssm-ID: 187717 [Multi-domain] Cd Length: 196 Bit Score: 326.83 E-value: 4.01e-114
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| purU | PRK13010 | formyltetrahydrofolate deformylase; Reviewed |
3-287 | 4.06e-105 | |||||
formyltetrahydrofolate deformylase; Reviewed Pssm-ID: 139334 [Multi-domain] Cd Length: 289 Bit Score: 307.49 E-value: 4.06e-105
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| PLN02828 | PLN02828 | formyltetrahydrofolate deformylase |
32-287 | 2.46e-72 | |||||
formyltetrahydrofolate deformylase Pssm-ID: 178422 Cd Length: 268 Bit Score: 223.47 E-value: 2.46e-72
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| PurN | COG0299 | Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and ... |
94-286 | 2.22e-44 | |||||
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and metabolism]; Folate-dependent phosphoribosylglycinamide formyltransferase PurN is part of the Pathway/BioSystem: Purine biosynthesis Pssm-ID: 440068 [Multi-domain] Cd Length: 202 Bit Score: 149.41 E-value: 2.22e-44
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| Formyl_trans_N | pfam00551 | Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ... |
94-269 | 9.72e-41 | |||||
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide transformylase catalyzes the third step in de novo purine biosynthesis, the transfer of a formyl group to 5'-phosphoribosylglycinamide. Formyltetrahydrofolate deformylase produces formate from formyl- tetrahydrofolate. Methionyl-tRNA formyltransferase transfers a formyl group onto the amino terminus of the acyl moiety of the methionyl aminoacyl-tRNA. Inclusion of the following members is supported by PSI-blast. HOXX_BRAJA (P31907) contains a related domain of unknown function. PRTH_PORGI (P46071) contains a related domain of unknown function. Y09P_MYCTU (Q50721) contains a related domain of unknown function. Pssm-ID: 395436 [Multi-domain] Cd Length: 181 Bit Score: 139.35 E-value: 9.72e-41
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| FMT_core_GART | cd08645 | Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); ... |
116-271 | 3.24e-40 | |||||
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); Phosphoribosylglycinamide formyltransferase, also known as GAR transformylase or GART, is an essential enzyme that catalyzes the third step in de novo purine biosynthesis. This enzyme uses formyl tetrahydrofolate as a formyl group donor to produce 5'-phosphoribosyl-N-formylglycinamide. In prokaryotes, GART is a single domain protein but in most eukaryotes it is the C-terminal portion of a large multifunctional protein which also contains GAR synthetase and aminoimidazole ribonucleotide synthetase activities. Pssm-ID: 187714 [Multi-domain] Cd Length: 183 Bit Score: 137.90 E-value: 3.24e-40
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| FMT_core | cd08369 | Formyltransferase, catalytic core domain; Formyltransferase, catalytic core domain. The ... |
121-271 | 2.44e-33 | |||||
Formyltransferase, catalytic core domain; Formyltransferase, catalytic core domain. The proteins of this superfamily contain a formyltransferase domain that hydrolyzes the removal of a formyl group from its substrate as part of a multistep transfer mechanism, and this alignment model represents the catalytic core of the formyltransferase domain. This family includes the following known members; Glycinamide Ribonucleotide Transformylase (GART), Formyl-FH4 Hydrolase, Methionyl-tRNA Formyltransferase, ArnA, and 10-Formyltetrahydrofolate Dehydrogenase (FDH). Glycinamide Ribonucleotide Transformylase (GART) catalyzes the third step in de novo purine biosynthesis, the transfer of a formyl group to 5'-phosphoribosylglycinamide. Formyl-FH4 Hydrolase catalyzes the hydrolysis of 10-formyltetrahydrofolate (formyl-FH4) to FH4 and formate. Methionyl-tRNA Formyltransferase transfers a formyl group onto the amino terminus of the acyl moiety of the methionyl aminoacyl-tRNA, which plays important role in translation initiation. ArnA is required for the modification of lipid A with 4-amino-4-deoxy-l-arabinose (Ara4N) that leads to resistance to cationic antimicrobial peptides (CAMPs) and clinical antimicrobials such as polymyxin. 10-formyltetrahydrofolate dehydrogenase (FDH) catalyzes the conversion of 10-formyltetrahydrofolate, a precursor for nucleotide biosynthesis, to tetrahydrofolate. Members of this family are multidomain proteins. The formyltransferase domain is located at the N-terminus of FDH, Methionyl-tRNA Formyltransferase and ArnA, and at the C-terminus of Formyl-FH4 Hydrolase. Prokaryotic Glycinamide Ribonucleotide Transformylase (GART) is a single domain protein while eukaryotic GART is a trifunctional protein that catalyzes the second, third and fifth steps in de novo purine biosynthesis. Pssm-ID: 187712 [Multi-domain] Cd Length: 173 Bit Score: 120.09 E-value: 2.44e-33
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| PurN | TIGR00639 | phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model ... |
94-278 | 4.39e-32 | |||||
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model describes phosphoribosylglycinamide formyltransferase (GAR transformylase), one of several proteins in formyl_transf (pfam00551). This enzyme uses formyl tetrahydrofolate as a formyl group donor to produce 5'-phosphoribosyl-N-formylglycinamide. PurT, a different GAR transformylase, uses ATP and formate rather than formyl tetrahydrofolate. Experimental proof includes complementation of E. coli purN mutants by orthologs from vertebrates (where it is a domain of a multifunctional protein), Bacillus subtilis, and Arabidopsis. No archaeal example was detected. In phylogenetic analyses, the member from Saccharomyces cerevisiae shows a long branch length but membership in the family, while the formyltetrahydrofolate deformylases form a closely related outgroup. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis] Pssm-ID: 161973 [Multi-domain] Cd Length: 190 Bit Score: 117.09 E-value: 4.39e-32
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| ACT_F4HF-DF | cd04875 | N-terminal ACT domain of formyltetrahydrofolate deformylase (F4HF-DF; formyltetrahydrofolate ... |
10-85 | 2.23e-28 | |||||
N-terminal ACT domain of formyltetrahydrofolate deformylase (F4HF-DF; formyltetrahydrofolate hydrolase); This CD includes the N-terminal ACT domain of formyltetrahydrofolate deformylase (F4HF-DF; formyltetrahydrofolate hydrolase) which catalyzes the hydrolysis of 10-formyltetrahydrofolate (formyl-FH4) to FH4 and formate. Formyl-FH4 hydrolase generates the formate that is used by purT-encoded 5'-phosphoribosylglycinamide transformylase for step three of de novo purine nucleotide synthesis. Formyl-FH4 hydrolase, a hexamer which is activated by methionine and inhibited by glycine, is proposed to regulate the balance FH4 and C1-FH4 in response to changing growth conditions. Members of this CD belong to the superfamily of ACT regulatory domains. Pssm-ID: 153147 [Multi-domain] Cd Length: 74 Bit Score: 103.79 E-value: 2.23e-28
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| PLN02331 | PLN02331 | phosphoribosylglycinamide formyltransferase |
141-278 | 3.91e-13 | |||||
phosphoribosylglycinamide formyltransferase Pssm-ID: 177965 [Multi-domain] Cd Length: 207 Bit Score: 66.64 E-value: 3.91e-13
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| PLN02285 | PLN02285 | methionyl-tRNA formyltransferase |
169-256 | 1.82e-10 | |||||
methionyl-tRNA formyltransferase Pssm-ID: 215159 [Multi-domain] Cd Length: 334 Bit Score: 60.48 E-value: 1.82e-10
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| FMT_core_Met-tRNA-FMT_N | cd08646 | Methionyl-tRNA formyltransferase, N-terminal hydrolase domain; Methionyl-tRNA ... |
134-255 | 3.05e-10 | |||||
Methionyl-tRNA formyltransferase, N-terminal hydrolase domain; Methionyl-tRNA formyltransferase (Met-tRNA-FMT), N-terminal formyltransferase domain. Met-tRNA-FMT transfers a formyl group from N-10 formyltetrahydrofolate to the amino terminal end of a methionyl-aminoacyl-tRNA acyl moiety, yielding formyl-Met-tRNA. Formyl-Met-tRNA plays essential role in protein translation initiation by forming complex with IF2. The formyl group plays a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and by impairing its binding to EFTU-GTP. The N-terminal domain contains a Rossmann fold and it is the catalytic domain of the enzyme. Pssm-ID: 187715 [Multi-domain] Cd Length: 204 Bit Score: 58.61 E-value: 3.05e-10
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| Fmt | COG0223 | Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis]; |
135-260 | 1.02e-08 | |||||
Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis]; Pssm-ID: 439993 [Multi-domain] Cd Length: 308 Bit Score: 55.11 E-value: 1.02e-08
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| FMT_core_like_5 | cd08823 | Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
96-239 | 4.38e-07 | |||||
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme. Pssm-ID: 187725 [Multi-domain] Cd Length: 177 Bit Score: 48.98 E-value: 4.38e-07
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| FMT_core_like_3 | cd08653 | Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
171-245 | 4.69e-07 | |||||
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme. Pssm-ID: 187721 [Multi-domain] Cd Length: 152 Bit Score: 48.36 E-value: 4.69e-07
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| FMT_core_ArnA_N | cd08644 | ArnA, N-terminal formyltransferase domain; ArnA_N: ArnA is a bifunctional enzyme required for ... |
130-268 | 5.06e-07 | |||||
ArnA, N-terminal formyltransferase domain; ArnA_N: ArnA is a bifunctional enzyme required for the modification of lipid A with 4-amino-4-deoxy-L-arabinose (Ara4N) that leads to resistance to cationic antimicrobial peptides (CAMPs) and clinical antimicrobials such as polymyxin. The C-terminal dehydrogenase domain of ArnA catalyzes the oxidative decarboxylation of UDP-glucuronic acid (UDP-GlcUA) to UDP-4-keto-arabinose (UDP-Ara4O), while the N-terminal formyltransferase domain of ArnA catalyzes the addition of a formyl group to UDP-4-amino-4-deoxy-L-arabinose (UDP-L-Ara4N) to form UDP-L-4-formamido-arabinose (UDP-L-Ara4FN). This domain family represents the catalytic core of the N-terminal formyltransferase domain. The formyltransferase also contains a smaller C-terminal domain the may be involved in substrate binding. ArnA forms a hexameric structure, in which the dehydrogenase domains are arranged at the center of the particle with the transformylase domains on the outside of the particle. Pssm-ID: 187713 [Multi-domain] Cd Length: 203 Bit Score: 49.27 E-value: 5.06e-07
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| ACT | pfam01842 | ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ... |
10-69 | 6.59e-07 | |||||
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to a wide range of metabolic enzymes that are regulated by amino acid concentration. Pairs of ACT domains bind specifically to a particular amino acid leading to regulation of the linked enzyme. The ACT domain is found in: D-3-phosphoglycerate dehydrogenase EC:1.1.1.95, which is inhibited by serine. Aspartokinase EC:2.7.2.4, which is regulated by lysine. Acetolactate synthase small regulatory subunit, which is inhibited by valine. Phenylalanine-4-hydroxylase EC:1.14.16.1, which is regulated by phenylalanine. Prephenate dehydrogenase EC:4.2.1.51. formyltetrahydrofolate deformylase EC:3.5.1.10, which is activated by methionine and inhibited by glycine. GTP pyrophosphokinase EC:2.7.6.5 Pssm-ID: 426468 [Multi-domain] Cd Length: 66 Bit Score: 45.76 E-value: 6.59e-07
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| FMT_core_like_6 | cd08820 | Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
152-256 | 2.88e-05 | |||||
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme. Pssm-ID: 187722 [Multi-domain] Cd Length: 173 Bit Score: 43.58 E-value: 2.88e-05
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| ACT | cd02116 | ACT domains are commonly involved in specifically binding an amino acid or other small ligand ... |
11-60 | 7.80e-05 | |||||
ACT domains are commonly involved in specifically binding an amino acid or other small ligand leading to regulation of the enzyme; Members of this CD belong to the superfamily of ACT regulatory domains. Pairs of ACT domains are commonly involved in specifically binding an amino acid or other small ligand leading to regulation of the enzyme. The ACT domain has been detected in a number of diverse proteins; some of these proteins are involved in amino acid and purine biosynthesis, phenylalanine hydroxylation, regulation of bacterial metabolism and transcription, and many remain to be characterized. ACT domain-containing enzymes involved in amino acid and purine synthesis are in many cases allosteric enzymes with complex regulation enforced by the binding of ligands. The ACT domain is commonly involved in the binding of a small regulatory molecule, such as the amino acids L-Ser and L-Phe in the case of D-3-phosphoglycerate dehydrogenase and the bifunctional chorismate mutase-prephenate dehydratase enzyme (P-protein), respectively. Aspartokinases typically consist of two C-terminal ACT domains in a tandem repeat, but the second ACT domain is inserted within the first, resulting in, what is normally the terminal beta strand of ACT2, formed from a region N-terminal of ACT1. ACT domain repeats have been shown to have nonequivalent ligand-binding sites with complex regulatory patterns such as those seen in the bifunctional enzyme, aspartokinase-homoserine dehydrogenase (ThrA). In other enzymes, such as phenylalanine hydroxylases, the ACT domain appears to function as a flexible small module providing allosteric regulation via transmission of conformational changes, these conformational changes are not necessarily initiated by regulatory ligand binding at the ACT domain itself. ACT domains are present either singularly, N- or C-terminal, or in pairs present C-terminal or between two catalytic domains. Unique to cyanobacteria are four ACT domains C-terminal to an aspartokinase domain. A few proteins are composed almost entirely of ACT domain repeats as seen in the four ACT domain protein, the ACR protein, found in higher plants; and the two ACT domain protein, the glycine cleavage system transcriptional repressor (GcvR) protein, found in some bacteria. Also seen are single ACT domain proteins similar to the Streptococcus pneumoniae ACT domain protein (uncharacterized pdb structure 1ZPV) found in both bacteria and archaea. Purportedly, the ACT domain is an evolutionarily mobile ligand binding regulatory module that has been fused to different enzymes at various times. Pssm-ID: 153139 [Multi-domain] Cd Length: 60 Bit Score: 39.97 E-value: 7.80e-05
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| GcvR | COG2716 | Glycine cleavage system regulator GcvR [Amino acid transport and metabolism]; |
8-59 | 9.15e-05 | |||||
Glycine cleavage system regulator GcvR [Amino acid transport and metabolism]; Pssm-ID: 442029 [Multi-domain] Cd Length: 174 Bit Score: 42.13 E-value: 9.15e-05
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| PRK06988 | PRK06988 | formyltransferase; |
108-268 | 3.88e-04 | |||||
formyltransferase; Pssm-ID: 235902 [Multi-domain] Cd Length: 312 Bit Score: 41.22 E-value: 3.88e-04
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| ACT_Af1403 | cd04874 | N-terminal ACT domain of the yet uncharacterized, small (~133 a.a.), putative amino acid ... |
11-56 | 5.30e-04 | |||||
N-terminal ACT domain of the yet uncharacterized, small (~133 a.a.), putative amino acid binding protein, Af1403, and related domains; This CD includes the N-terminal ACT domain of the yet uncharacterized, small (~133 a.a.), putative amino acid binding protein, Af1403, from Archaeoglobus fulgidus and other related archeal ACT domains. Members of this CD belong to the superfamily of ACT regulatory domains. Pssm-ID: 153146 [Multi-domain] Cd Length: 72 Bit Score: 37.66 E-value: 5.30e-04
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| PRK08125 | PRK08125 | bifunctional UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronic acid oxidase ... |
176-239 | 3.61e-03 | |||||
bifunctional UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronic acid oxidase ArnA; Pssm-ID: 236156 [Multi-domain] Cd Length: 660 Bit Score: 38.81 E-value: 3.61e-03
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